Coordinated collagen and muscle protein synthesis in human patella tendon and quadriceps muscle after exercise

Benjamin F. Miller; Jens L. Olesen; Mette Hansen; Simon Døssing; Regina M. Crameri; Rasmus J. Welling; Henning Langberg; Allan Flyvbjerg; Michael Kjaer; John A. Babraj; Michael J. Rennie

doi:10.1113/jphysiol.2005.093690

journal article Sep 01, 2005

Coordinated collagen and muscle protein synthesis in human patella tendon and quadriceps muscle after exercise

Jens L. Olesen Mette Hansen Simon Døssing Regina M. Crameri Rasmus J. Welling Henning Langberg Allan Flyvbjerg Michael Kjaer John A. Babraj Michael J. Rennie

The Journal of Physiology Vol. 567 No. 3 pp. 1021-1033 · Wiley

View at Publisher Save 10.1113/jphysiol.2005.093690

Abstract

We hypothesized that an acute bout of strenuous, non‐damaging exercise would increase rates of protein synthesis of collagen in tendon and skeletal muscle but these would be less than those of muscle myofibrillar and sarcoplasmic proteins. Two groups (n= 8 and 6) of healthy young men were studied over 72 h after 1 h of one‐legged kicking exercise at 67% of maximum workload (Wmax). To label tissue proteins in muscle and tendon primed, constant infusions of [1‐13C]leucine or [1‐13C]valine and flooding doses of [15N] or [13C]proline were given intravenously, with estimation of labelling in target proteins by gas chromatography–mass spectrometry. Patellar tendon and quadriceps biopsies were taken in exercised and rested legs at 6, 24, 42 or 48 and 72 h after exercise. The fractional synthetic rates of all proteins were elevated at 6 h and rose rapidly to peak at 24 h post exercise (tendon collagen (0.077% h−1), muscle collagen (0.054% h−1), myofibrillar protein (0.121% h−1), and sarcoplasmic protein (0.134% h−1)). The rates decreased toward basal values by 72 h although rates of tendon collagen and myofibrillar protein synthesis remained elevated. There was no tissue damage of muscle visible on histological evaluation. Neither tissue microdialysate nor serum concentrations of IGF‐I and IGF binding proteins (IGFBP‐3 and IGFBP‐4) or procollagen type I N‐terminal propeptide changed from resting values. Thus, there is a rapid increase in collagen synthesis after strenuous exercise in human tendon and muscle. The similar time course of changes of protein synthetic rates in different cell types supports the idea of coordinated musculotendinous adaptation.

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Details

Published: Sep 01, 2005
Vol/Issue: 567(3)
Pages: 1021-1033
License: View

Authors

B

Benjamin F. Miller

From the Department of Physical Chemistry in the Laboratories of Physiology, Harvard Medical School, Boston

Institute of Sports Medicine, Bispebjerg Hospital and Center of Healthy Aging, Faculty of Health Science, University of Copenhagen, Copenhagen; and

Cite This Article

Benjamin F. Miller, Jens L. Olesen, Mette Hansen, et al. (2005). Coordinated collagen and muscle protein synthesis in human patella tendon and quadriceps muscle after exercise. The Journal of Physiology, 567(3), 1021-1033. https://doi.org/10.1113/jphysiol.2005.093690

Coordinated collagen and muscle protein synthesis in human patella tendon and quadriceps muscle after exercise

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